Structure of calmodulin refined at 2.2 Å resolution

YS Babu, CE Bugg, WJ Cook - Journal of molecular biology, 1988 - Elsevier
The crystal structure of mammalian calmodulin has been refined at 2.2 Å (1 Å= 0.1 nm)
resolution using a restrained least-squares method. The final crystallographic R-factor …

Metal-ion binding and the molecular conformational properties of α lactalbumi

MJ Kronman, GD Fasman - Critical reviews in biochemistry and …, 1989 - Taylor & Francis
The subject of this review, the milk-specific protein a lactalbumin (a LA), is the regulatory
component of the lactose synthase complex which catalyzes the biosynthesis of lactose in …

[图书][B] Chemical reagents for protein modification

RL Lundblad - 2004 - taylorfrancis.com
Revised and updated, Chemical Reagents for Protein Modification, Third Edition is an
encyclopedic work describing the many approaches to the site-specific modification of …

[图书][B] Handbook of affinity chromatography

T Kline - 1993 - taylorfrancis.com
Outlining the fundamental principles by which all interactions occur, this reference focuses
on harnessing the biochemistry of bioorganic compounds in order to separate them …

Acetaldehyde and microtubules.

DJ Tuma, SL Smith, MF Sorrell - Annals of the New York Academy of …, 1991 - europepmc.org
Acetaldehyde covalently binds to tubulin to form stable and unstable adducts. Although
tubulin has numerous lysine residues available to react with acetaldehyde, a key highly …

Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex

WJ Cook, LJ Walter, MR Walter - Biochemistry, 1994 - ACS Publications
Revised Manuscript Received October 18, 1994® abstract; The crystal structure of
calmodulin (CaM) boundto trifluoperazine (TFP) has been determined and refined to a …

Apocalmodulin and Ca2+ Calmodulin Bind to the Same Region on the Skeletal Muscle Ca2+ Release Channel

CP Moore, G Rodney, JZ Zhang… - Biochemistry, 1999 - ACS Publications
The skeletal muscle Ca2+ release channel (RYR1) is regulated by calmodulin in both its
Ca2+-free (apocalmodulin) and Ca2+-bound (Ca2+ calmodulin) states. Apocalmodulin is an …

[37] Recognition and characterization of calmodulin-binding sequences in peptides and proteins

S Erickson-Viitanen, WF Degrado - Methods in enzymology, 1987 - Elsevier
Publisher Summary This chapter provides methods for the recognition and analysis of basic,
amphiphilic calmodulin-binding regions in peptides and proteins. The first calmodulin …

Mechanism of2-Chloro-(. epsilon.-amino-Lys75)-[6-[4-(N, N-diethylamino) phenyl]-1, 3, 5-triazin-4-yl] calmodulin Interactions with Smooth Muscle Myosin Light Chain …

K Torok, DR Trentham - Biochemistry, 1994 - ACS Publications
Revised Manuscript Received August 12, 1994® abstract: The mechanism of the
interactions of 2-chloro-(€-amino-Lys75)-[6-[4-(7V, A-diethylamino) phenyl]-1, 3, 5-triazin-4 …

[HTML][HTML] Determination of the side chain pKa values of the lysine residues in calmodulin.

M Zhang, HJ Vogel - Journal of Biological Chemistry, 1993 - Elsevier
The 7 Lys residues in mammalian calmodulin (CaM) were reductively methylated with 13C-
enriched formaldehyde and studied by (1H, 13C)-heteronuclear multiple quantum …